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1CVL

CRYSTAL STRUCTURE OF BACTERIAL LIPASE FROM CHROMOBACTERIUM VISCOSUM ATCC 6918

Experimental procedure
Source typeSYNCHROTRON
Source detailsMPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron siteMPG/DESY, HAMBURG
BeamlineBW6
Temperature [K]293
Detector technologyIMAGE PLATE
Collection date1993-11
DetectorMARRESEARCH
Spacegroup nameP 21 21 2
Unit cell lengths41.080, 156.820, 43.610
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution8.000 - 1.600
R-factor0.178

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Rwork0.178
Structure solution methodMIR
RMSD bond length0.021
RMSD bond angle0.044
Data reduction softwareMOSFLM
Data scaling softwareCCP4
Phasing softwareMLPHARE
Refinement softwarePROLSQ
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.640
High resolution limit [Å]1.6001.600
Rmerge0.0530.220

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Total number of observations87722

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Number of reflections33644
<I/σ(I)>8.53.1
Completeness [%]88.073.7
Redundancy2.61.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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6.4292

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PROTEIN WAS CRYSTALLIZED FROM 10-14 % PEG 4000, 10-14 % MPD, 100 MM CITRATE/PHOSPHATE BUFFER, PH 6.4
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11droplipase15 (mg/ml)
21dropTris-HCl5 (mM)
31dropn-octyl-beta-D-glycopyranoside0.25 (%(w/v))
41reservoirPEG400014 (%(w/v))
51reservoirMPD10-14 (%(v/v))
61reservoircitrate-phosphate100 (mM)

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